Research workbench
Crystal structure of human fto in complex with acylhydrazine inhibitor 21
Analyse Crystal structure of human fto in complex with acylhydrazine inhibitor 21 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4CXY
- Type
- protein
- Length
- 436 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-ketoglutarate-dependent dioxygenase fto
- EC
- 1.14.11.-
- UniProt
- Q9C0B1
- Ligands
- DGR, NI
- Pockets
- 5 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-ketoglutarate-dependent dioxygenase fto (EC 1.14.11.-) | protein | 436 | 39% helix, 20% strand | Q9C0B1 |
Ligands and binding sites
- DGR · (E)-4-(2-Nicotinoylhydrazinyl)-4-oxobut-2-enoic acid · ligand · chains A
- NI · Nickel (II) ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 110 | 0.74 | 0.94 | 20 | empty |
| 2 | 325 | 0.70 | 0.83 | 40 | DGR, NI |
| 3 | 52 | 0.40 | 0.82 | 18 | empty |
| 4 | 110 | 0.37 | 0.74 | 19 | empty |
| 5 | 57 | 0.26 | 0.73 | 14 | empty |
Compared structures
- 4CXY · Crystal structure of human FTO in complex with acylhydrazine inhibitor 21 · the same entry in another collection · chain A against A, TM-score 1.00
- Q9C0B1 · AlphaFold monomer V2.0 prediction for alpha-ketoglutarate-dependent dioxygenase fto… · a predicted model of the same protein · chain A against A, TM-score 0.99
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q9C0B1
- Elsewhere: RCSB PDB 4CXY · PDBe 4CXY · UniProt Q9C0B1
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